Hengchang Zang


Group leader: Prof. Hengchang Zang

Affiliation: School of Pharmaceutical Sciences, Shandong University, China

Research Topics: Process analysis technology, Near infrared spectroscopy, Aquaphotomics

Contact: zanghcw@126.com

NIRS is a modern analytical technique that makes use of the material information contained in the near infrared spectrum region and relies on chemometrics and computer technology to carry out qualitative and quantitative analysis of organic substances. It is one of the most important tools in PAT technology. NIRS has become one of the most rapidly developed new analytical techniques in the past decade due to its advantages of fast analysis speed, no pretreatment, no pollution, and simultaneous analysis of multiple components.

Drug quality and its uniformity is one of the important basic characteristics of drugs, and it is the core of drug efficacy and drug risk management. Many advanced pharmaceutical companies have adopted NIR spectroscopy for quality analysis and control of the whole process. However, the application of NIR spectroscopy in the pharmaceutical field is still in the research stage, and the common problems of many methodologies need to be further studied and understood. It is necessary to conduct theoretical discussion and experimental research on how to integrate the implementation of engineering, drug registration regulations, and the restrictions of GMP clauses. The consistency of drug efficacy and the improvement of drug re-registration standards all need the support of NIR technology. Therefore, in recent years, our research group has been devoted to the theoretical exploration and application research of the application of NIR spectroscopy in the pharmaceutical field.

Aquaphotomics related work

Hydration plays an important role in the stability of protein structure and function. The dynamic characteristics of hydration play a key role in biochemical processes, including protein folding, enzyme function, and molecular recognition. Protein purification is affected by hydration and dehydration. We used NIR spectroscopy to study the morphological changes of the hydration layer around protein molecules and detected the network structure of hydrogen bond water around protein molecules by changing the protein concentration, thus providing theoretical support for the stability of protein structure.